3pdq
From Proteopedia
(Difference between revisions)
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- | + | ==Crystal structure of JMJD2A complexed with bipyridyl inhibitor== | |
- | + | <StructureSection load='3pdq' size='340' side='right' caption='[[3pdq]], [[Resolution|resolution]] 1.99Å' scene=''> | |
- | + | == Structural highlights == | |
- | ==Function== | + | <table><tr><td colspan='2'>[[3pdq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PDQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PDQ FirstGlance]. <br> |
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=KC6:4-[(2-AMINOETHYL)CARBAMOYL]-2,2-BIPYRIDINE-4-CARBOXYLIC+ACID'>KC6</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3njy|3njy]], [[2wwj|2wwj]], [[2vd7|2vd7]], [[2oq7|2oq7]], [[2ox0|2ox0]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KDM4A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3pdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pdq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pdq RCSB], [http://www.ebi.ac.uk/pdbsum/3pdq PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
[[http://www.uniprot.org/uniprot/KDM4A_HUMAN KDM4A_HUMAN]] Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively.<ref>PMID:16024779</ref> <ref>PMID:16603238</ref> <ref>PMID:21694756</ref> Isoform 2: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain.<ref>PMID:16024779</ref> <ref>PMID:16603238</ref> <ref>PMID:21694756</ref> | [[http://www.uniprot.org/uniprot/KDM4A_HUMAN KDM4A_HUMAN]] Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively.<ref>PMID:16024779</ref> <ref>PMID:16603238</ref> <ref>PMID:21694756</ref> Isoform 2: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain.<ref>PMID:16024779</ref> <ref>PMID:16603238</ref> <ref>PMID:21694756</ref> | ||
- | == | + | ==See Also== |
- | [[ | + | *[[Jumonji domain-containing protein 2A|Jumonji domain-containing protein 2A]] |
- | + | == References == | |
- | == | + | <references/> |
- | + | __TOC__ | |
+ | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
- | [[Category: Chang, K H | + | [[Category: Chang, K H]] |
- | [[Category: Clifton, I J | + | [[Category: Clifton, I J]] |
- | [[Category: King, O N.F | + | [[Category: King, O N.F]] |
- | [[Category: McDonough, M A | + | [[Category: McDonough, M A]] |
- | [[Category: Rose, N R | + | [[Category: Rose, N R]] |
- | [[Category: Schofield, C J | + | [[Category: Schofield, C J]] |
[[Category: 2-oxoglutarate]] | [[Category: 2-oxoglutarate]] | ||
[[Category: Alpha-ketoglutarate]] | [[Category: Alpha-ketoglutarate]] |
Revision as of 06:21, 25 December 2014
Crystal structure of JMJD2A complexed with bipyridyl inhibitor
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Categories: Human | Chang, K H | Clifton, I J | King, O N.F | McDonough, M A | Rose, N R | Schofield, C J | 2-oxoglutarate | Alpha-ketoglutarate | Chromatin regulator | Demethylation | Dioxygenase | Iron | Jmjc domain | Nucleus | Oxidoreductase | Oxidoreductase-oxidoreductase inhibitor complex | Transcription